@phdthesis{oai:nagasaki-u.repo.nii.ac.jp:00000607,
 author = {SARWAR, MOHAMMAD TANVIR},
 month = {Mar},
 note = {Prevotella intermedia, a gram-negative anaerobic rod, is frequently observed in subgingival polymicrobial biofilm from adults with chronic periodontitis. Peptidases in periodontopathic bacteria are considered to function as etiological reagents. Pre. intermedia OMA14 cells abundantly express an unidentified cysteine peptidase specific for Arg-4-methycoumaryl-7- amide (MCA). BAU17746 (locus tag, PIOMA14_I_1238) and BAU18827 (locus tag, PIOMA14_II_0322) emerged as candidates of this peptidase from the substrate specificity and sequence similarity with C69-family Streptococcus gordonii Arg-aminopeptidase. The recombinant form of the former solely exhibited hydrolyzing activity toward Arg-MCA, and BAU17746 possesses a 26.6% amino acid identity with the C69-family Lactobacillus helveticus dipeptidase A. It was found that BAU17746 as well as L. helveticus dipeptidase A was a P1-position Arg-specific dipeptidase A, although the L. helveticus entity, a representative of the C69 family, had been reported to be specific for Leu and Phe. The fulllength form of BAU17746 was intramolecularly processed to a mature form carrying the N-terminus of Cys15. In conclusion, the marked Arg-MCA-hydrolyzing activity in Pre. intermedia was mediated by BAU17746 belonging to the C69-family dipeptidase A, in which the mature form carries an essential cysteine at the N-terminus., 長崎大学学位論文 学位記番号:博(医歯薬)甲第1215号 学位授与年月日:令和2年3月19日, Author: Mohammad Tanvir Sarwar, Yuko Ohara-Nemoto, Takeshi Kobayakawa, Mariko Naito and Takayuki K. Nemoto, Citation: Biological Chemistry, 401(5),  pp. 629-642 ; 2020, Nagasaki University (長崎大学), 博士(歯学) (2020-03-19)},
 school = {Nagasaki University (長崎大学)},
 title = {Characterization of substrate specificity and novel autoprocessing mechanism of dipeptidase A from Prevotella intermedia},
 year = {2020}
}